Evidence map›Paper›PMID 26717260›Full record

ArticleJournal of inorganic biochemistry2016

Investigating the position of the hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis and inhibitor binding.

Mahesh Aitha, Abraham J Moller, Indra D Sahu, Masaki Horitani, David L Tierney, Michael W Crowder

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of inorganic biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Mahesh AithaDepartment of Chemistry and Biochemistry, Miami University, 650 East High Street, Oxford, OH 45056, USA.
Abraham J MollerDepartment of Chemistry and Biochemistry, Miami University, 650 East High Street, Oxford, OH 45056, USA.
Indra D SahuDepartment of Chemistry and Biochemistry, Miami University, 650 East High Street, Oxford, OH 45056, USA.
Masaki HoritaniDepartment of Chemistry, Northwestern University, Evanston, IL 60208-3113, USA.
David L TierneyDepartment of Chemistry and Biochemistry, Miami University, 650 East High Street, Oxford, OH 45056, USA.
Michael W CrowderDepartment of Chemistry and Biochemistry, Miami University, 650 East High Street, Oxford, OH 45056, USA. Electronic address: crowdemw@miamioh.edu.

Funding

Coboglobins-Cobalt-Substituted Hemoglobins and MyoglobinR01GM111097 · NIGMS · NORTHWESTERN UNIVERSITY · PI HOFFMAN, BRIAN M · 2014 to 2025
$6.7M
NIGMS NIH HHS GM111097NIGMS NIH HHS R01 GM111097
6 · The paper itself

Abstract

In an effort to examine the relative position of a hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis, rapid freeze quench double electron electron resonance (RFQ-DEER) spectroscopy was used. A doubly-labeled mutant of NDM-1, which had one spin label on the invariant loop at position 69 and another label at position 235, was prepared and characterized. The reaction of the doubly spin labeled mutant with chromacef was freeze quenched at 500μs and 10ms. DEER results showed that the average distance between labels decreased by 4Å in the 500μs quenched sample and by 2Å in the 10ms quenched sample, as compared to the distance in the unreacted enzyme, although the peaks corresponding to distance distributions were very broad. DEER spectra with the doubly spin labeled enzyme with two inhibitors showed that the distance between the loop residue at position 69 and the spin label at position 235 does not change upon inhibitor binding. This study suggests that the hairpin loop in NDM-1 moves over the metal ion during the catalysis and then moves back to its original position after hydrolysis, which is consistent with a previous hypothesis based on NMR solution studies on a related metallo-β-lactamase. This study also demonstrates that this loop motion occurs in the millisecond time domain.

Indexed as

beta-Lactamase Inhibitorsbeta-LactamasesCatalysisMolecular Dynamics Simulationbeta-Lactamase Inhibitorsbeta-LactamasesDEER spectroscopyMetallo-β-lactamaseRapid freeze quenchSite specific spin labeling

Identifiers

PMID26717260
PMCPMC4843777

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.